The overall objectives of research being carried out in our laboratory are to study the chemistry, regulation of biosynthesis and mechanism of secretion of epithelial mucins and the chemistry of membranous components of the cell. Specific goals for this project include studies on an ovarian cyst glycoprotein and the effects of isoproterenol on glycosyltransferase activities in rat parotid gland. Our laboratory has been successful in isolating several oligosaccharides from an ovarian cyst glycoprotein. This is a unique cyst in that it was obtained from an AB secretor as an insoluble secretion, but had no ABH blood group activity. Assays with galactosyltransferase showed no acceptor activity in the cyst glycoprotein until sialic acid had been removed. These data support the proposition that the addition of sialic acid terminates the further addition of sugars to a growing oligosaccharide chain. Isoproterenol treatment causes a demonstrable increase in the specific activity of the galactosyl:N-acetylglucosamine transferase, but not in the galactosyl:N-acetylgalactosamine transferase. Specific activities of the former increase 6-10 fold after about a week of treatment (5 mg isoproterenol/animal/day, IP). Currently, we plan on performing subcellular distribution and EM studies to determine if this increase in activity is related to an increase in Golgi membranes. In addition, this transferase may increase during periods of cell division, which is consistent with previous studies on the developing rat pancreas (Carlson, David and Rutter, Arch. Biochem. Biophys., 142, 101 (1973).